Evidence map›Paper›PMID 23874229›Full record

ArticlePLoS genetics2013

Genome-scale co-evolutionary inference identifies functions and clients of bacterial Hsp90.

Maximilian O Press, Hui Li, Nicole Creanza, Günter Kramer, Christine Queitsch, Victor Sourjik, Elhanan Borenstein

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Hsp90, a team player in protein quality control and the stress response in bacteria.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Pervasive convergent evolution and extreme phenotypes define chaperone requirements of protein homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  7. Intermolecular Interactions between Hsp90 and Hsp70.Journal of molecular biology · 2019
    Article
  8. Article
  9. Review
  10. Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling.The Journal of biological chemistry · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Bacterial protein networks: properties and functions.Nature reviews. Microbiology · 2015
    Review
  15. Hsp90 promotes kinase evolution.Molecular biology and evolution · 2015
    Article
  16. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Maximilian O PressDepartment of Genome Sciences, University of Washington, Seattle, Washington, USA.
Hui Li
Nicole Creanza
Günter Kramer
Christine Queitsch
Victor Sourjik
Elhanan Borenstein
University of Washington · USHeidelberg University · DEDKFZ-ZMBH Alliance · DEStanford University · US

Funding

Thermally robust chemotaxis and thermotaxis in Escherichia coliR01GM082938 · NIGMS · PRINCETON UNIVERSITY · PI WINGREEN, NED S · 2008 to 2025
$5.5M
Does organismal robustness explain the missing heritability in complex diseases?DP2OD008371 · OD · UNIVERSITY OF WASHINGTON · PI QUEITSCH, CHRISTINE · 2011 to 2011
$2.3M
NCCIH NIH HHS DP2AT00780201NIGMS NIH HHS GM 082938-05NIGMS NIH HHS R01 GM082938NIH HHS DP2 OD008371NIH HHS DP2OD008371
6 · The paper itself

Abstract

The molecular chaperone Hsp90 is essential in eukaryotes, in which it facilitates the folding of developmental regulators and signal transduction proteins known as Hsp90 clients. In contrast, Hsp90 is not essential in bacteria, and a broad characterization of its molecular and organismal function is lacking. To enable such characterization, we used a genome-scale phylogenetic analysis to identify genes that co-evolve with bacterial Hsp90. We find that genes whose gain and loss were coordinated with Hsp90 throughout bacterial evolution tended to function in flagellar assembly, chemotaxis, and bacterial secretion, suggesting that Hsp90 may aid assembly of protein complexes. To add to the limited set of known bacterial Hsp90 clients, we further developed a statistical method to predict putative clients. We validated our predictions by demonstrating that the flagellar protein FliN and the chemotaxis kinase CheA behaved as Hsp90 clients in Escherichia coli, confirming the predicted role of Hsp90 in chemotaxis and flagellar assembly. Furthermore, normal Hsp90 function is important for wild-type motility and/or chemotaxis in E. coli. This novel function of bacterial Hsp90 agreed with our subsequent finding that Hsp90 is associated with a preference for multiple habitats and may therefore face a complex selection regime. Taken together, our results reveal previously unknown functions of bacterial Hsp90 and open avenues for future experimental exploration by implicating Hsp90 in the assembly of membrane protein complexes and adaptation to novel environments.

Indexed as

Bacterial ProteinsChemotaxisEscherichia coliEscherichia coli ProteinsFlagellaGenome, BacterialHistidine KinaseHSP90 Heat-Shock ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular ChaperonesMultiprotein ComplexesPhylogenySignal TransductionBacterial ProteinscheA protein, E coliEscherichia coli ProteinsFliN protein, BacteriaHistidine KinaseHSP90 Heat-Shock ProteinsMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsMolecular ChaperonesMultiprotein Complexes

Identifiers

PMID23874229
PMCPMC3708813
OpenAlexW2112488748

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.